Identification and characterization of a novel anthocyanin malonyltransferase from scarlet sage (Salvia splendens) flowers: an enzyme that is phylogenetically separated from other anthocyanin acyltransferases
| Autor: | Hirokazu Suzuki, Kazufumi Watanabe, Masa-atsu Yamaguchi, Shiro Nagae, Toru Nakayama, Tokuzo Nishino, Shin'ya Sawada |
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| Rok vydání: | 2004 |
| Předmět: |
DNA
Complementary Subfamily Sequence Homology Amino Acid biology Reverse Transcriptase Polymerase Chain Reaction Molecular Sequence Data food and beverages Flowers Cell Biology Plant Science biology.organism_classification Anthocyanins Flavonoid biosynthesis Biochemistry Acyltransferases Acyltransferase Acetyltransferase Complementary DNA Genetics Scarlet sage Amino Acid Sequence Salvia Cloning Molecular Peptide sequence |
| Zdroj: | The Plant Journal. 38:994-1003 |
| ISSN: | 1365-313X 0960-7412 |
| DOI: | 10.1111/j.1365-313x.2004.02101.x |
| Popis: | Anthocyanin acyltransferases (AATs) catalyze a regiospecific acyl transfer from acyl-CoA to the glycosyl moiety of anthocyanins, thus playing an important role in flower coloration. The known AATs are subfamily members of an acyltransferase family, the BAHD family, which play important roles in secondary metabolism in plants. Here, we describe the purification, characterization, and cDNA cloning of a novel anthocyanin malonyltransferase from scarlet sage (Salvia splendens) flowers. The purified enzyme (hereafter referred to as Ss5MaT2) is a monomeric 46-kDa protein that catalyzes the transfer of the malonyl group from malonyl-CoA to the 4"'-hydroxyl group of the 5-glucosyl moiety of anthocyanins. Thus, it is a malonyl-CoA:anthocyanin 5-glucoside 4"'-O-malonyltransferase. On the basis of the partial amino acid sequences of the purified enzyme, we isolated a cDNA that encodes an acyltransferase protein. The steady-state transcript level of the gene was the highest in recently opened, fully pigmented flowers and was also correlated with the trend observed for an AAT gene responsible for the first malonylation step during salvianin biosynthesis. Immunoprecipitation studies using antibodies against the recombinant acyltransferase protein corroborated the identity of this cDNA as that encoding Ss5MaT2. The deduced amino acid sequence of Ss5MaT2 showed a low similarity (22-24% identity) to those of AATs and lacked the AAT-specific signature sequence. A phylogenetic analysis suggested that Ss5MaT2 is more related to acetyl-CoA:benzylalcohol acetyltransferase (BEAT) rather than to AAT. This is another example in which enzymes with similar, although not identical, substrate evolved from different branches of the BAHD family. |
| Databáze: | OpenAIRE |
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